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1H, 13C, and 15N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family

Journal Contribution - Journal Article

The cryptic prophage CP-933P in Escherichia coli O157:H7 contains a parDE-like toxin-antitoxin module, the operator region of which is recognized by two flanking transcription regulators: PaaR2 (ParE associated Regulator), which forms part of the paaR2-paaA2-parE2 toxin-antitoxin operon and YdaS (COG4197), which is encoded in the opposite direction but shares the operator. Here we report the 1H, 15N and 13C backbone and side chain chemical shift assignments of YdaS from Escherichia coli O157:H7 in its free state. YdaS is a distinct relative to HigA antitoxins but behaves as a monomer in solution. The BMRB Accession Number is 27917.
Journal: Biomolecular NMR Assignments
ISSN: 1874-2718
Issue: 1
Volume: 14
Pages: 25-30
Number of pages: 6
Publication year:2020
Keywords:NMR spectroscopy, protein structure, Structural biology, Toxin-antitoxin module, Biochemistry/biophysics/molecular biology, Analytical, inorganic & nuclear chemistry